Bueno MT, Richard S (2013) SUMOylation negatively modulates target gene occupancy of the KDM5B, a histone lysine demethylase. Epigenetics 8, 1162-75 23970103

This page summarizes selected information from the record referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.

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K242-sm - JARID1B (human) ▲

Modsite: RAEAMNIkIEPEETT SwissProt Entrez-Gene Orthologous residues JARID1B (human): K242‑sm, JARID1B iso2 (human): K278‑sm, JARID1B (mouse): K242‑sm, JARID1B (rat): K242‑sm Characterization Methods used to characterize site in vivo:  electrophoretic mobility shift, immunoprecipitation, modification-specific antibody, mutation of modification site, western blotting Disease tissue studied:  bone cancer, breast cancer Relevant cell lines - cell types - tissues:  293 (epithelial), HEK293T (epithelial), MCF-7 (breast cell), U2OS (bone cell) Cellular systems studied:  cell lines Species studied:  human Upstream Regulation Potential in vivo enzymes for site:  Type Enzyme Evidence Notes SUMO LIGASE UBC9 (human) transfection of wild-type enzyme SUMO LIGASE CBX4 (human) co-immunoprecipitation, microscopy-colocalization, transfection of wild-type enzyme Treatments, proteins and their effect on site modification:  Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes PIAS4 (human) no change compared to control nocodazole increase hydroxyurea increase Downstream Regulation Effect of modification (function):  enzymatic activity, induced, molecular association, regulation Effect of modification (process):  transcription, induced Modification regulates interactions with:  Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays Disrupts Comments:  regulates JARID1B demethylase activity

K278-sm - JARID1B (human) ▲

Modsite: KEMKSSIkQEPIERK SwissProt Entrez-Gene Orthologous residues JARID1B (human): K278‑sm, JARID1B iso2 (human): K314‑sm, JARID1B (mouse): K278‑sm, JARID1B (rat): K278‑sm Characterization Methods used to characterize site in vivo:  electrophoretic mobility shift, immunoprecipitation, modification-specific antibody, mutation of modification site, western blotting Disease tissue studied:  bone cancer, breast cancer Relevant cell lines - cell types - tissues:  293 (epithelial), HEK293T (epithelial), MCF-7 (breast cell), U2OS (bone cell) Cellular systems studied:  cell lines Species studied:  human Upstream Regulation Potential in vivo enzymes for site:  Type Enzyme Evidence Notes SUMO LIGASE UBC9 (human) transfection of wild-type enzyme SUMO LIGASE CBX4 (human) co-immunoprecipitation, microscopy-colocalization, transfection of wild-type enzyme Treatments, proteins and their effect on site modification:  Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes PIAS4 (human) no change compared to control nocodazole increase hydroxyurea increase Downstream Regulation Effect of modification (function):  enzymatic activity, induced, molecular association, regulation Effect of modification (process):  transcription, induced Modification regulates interactions with:  Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays Disrupts Comments:  regulates JARID1B demethylase activity